ID A0A3B5Q0G0_XIPMA Unreviewed; 358 AA.
AC A0A3B5Q0G0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ataxin-7-like protein 3 {ECO:0000256|HAMAP-Rule:MF_03047};
DE AltName: Full=SAGA-associated factor 11 homolog {ECO:0000256|HAMAP-Rule:MF_03047};
GN Name=ATXN7L3 {ECO:0000256|HAMAP-Rule:MF_03047};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000024312.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000024312.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000024312.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the transcription regulatory histone acetylation
CC (HAT) complex SAGA, a multiprotein complex that activates transcription
CC by remodeling chromatin and mediating histone acetylation and
CC deubiquitination. Within the SAGA complex, participates in a subcomplex
CC that specifically deubiquitinates histone H2B. The SAGA complex is
CC recruited to specific gene promoters by activators, where it is
CC required for transcription. {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC complexes. Within the SAGA complex, participates to a subcomplex of
CC SAGA called the DUB module (deubiquitination module).
CC {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain forms part of the
CC 'catalytic lobe' of the SAGA deubiquitination module.
CC {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of
CC the SAGA deubiquitination module. {ECO:0000256|HAMAP-Rule:MF_03047}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000256|HAMAP-
CC Rule:MF_03047}.
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DR RefSeq; XP_014330657.1; XM_014475171.1.
DR RefSeq; XP_014330661.1; XM_014475175.1.
DR AlphaFoldDB; A0A3B5Q0G0; -.
DR Ensembl; ENSXMAT00000021596.1; ENSXMAP00000024312.1; ENSXMAG00000008271.2.
DR GeneID; 102236134; -.
DR KEGG; xma:102236134; -.
DR CTD; 368510; -.
DR GeneTree; ENSGT00940000158253; -.
DR OrthoDB; 5404108at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.140.1270; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR013243; SCA7_dom.
DR PANTHER; PTHR46367; ATAXIN-7-LIKE PROTEIN 3; 1.
DR PANTHER; PTHR46367:SF4; ATAXIN-7-LIKE PROTEIN 3; 1.
DR Pfam; PF08209; Sgf11; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|HAMAP-Rule:MF_03047};
KW Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03047};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03047};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03047};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_03047};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_03047};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03047};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_03047}.
FT DOMAIN 200..267
FT /note="SCA7"
FT /evidence="ECO:0000259|PROSITE:PS51505"
FT ZN_FING 84..105
FT /note="SGF11-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03047"
FT REGION 123..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39957 MW; 2AF9E50C5A2AC6C2 CRC64;
MKMEEKPLSG PDNTRLEALI QDVYSELVED ACLGLCFEVH RAVKQGYFFL DETDQDSIKE
FEIVDQPGVD IFGQVFNQWK NKECECPNCK RLIAASRFAP HLEKCLGMGR NSSRIANRRL
ATNNNISKSE SDQEDNDDLN DNDWSYGAEK KAKKRRPDKN QNSPRRSKSL KHKNGELGTS
LSSDPYKQYN YNAGISYESL GPNEIRSLLT TQCGVISEHT KRMCTRSHRC PQHTDDQRRA
IRLFLLGPSV PTLPDADVEG DSFDIPNGQA LLSRLQWEDF PDVSPTDSAS SKASTNHSDS
KRPKKKKRLD LSLNSGGGGV NMTGVSSSSC QSNISLSTKK KKPKTAAPSV SSIYDELN
//
